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Carbon Monoxide myoglobin

Since enthalpy changes can be obtained directly from measurement of heat absorption at constant pressure, even small values of AH for chemical and biochemical reactions can be measured using a micro-calorimeter.1112 Using the technique of pulsed acoustic calorimetry, changes during biochemical processes can be followed on a timescale of fractions of a millisecond. An example is the laser-induced dissociation of a carbon monoxide-myoglobin complex.13... [Pg.282]

An Analysis of the Carbon Monoxide Myoglobin Water Structure... [Pg.215]

Fiber R and M Karplus 1990. Enhanced Sampling in Molecular Dynamics Use of the Time-Dependent Hartree Approximation for a Simulation of Carbon Monoxide Diffusion through Myoglobin. Journal of the American Chemical Society 112 9161-9175. [Pg.650]

FIGURE 15.26 Oxygen and carbon monoxide binding to the heme group of myoglobin. [Pg.482]

Figure 6-3. Angles for bonding of oxygen and carbon monoxide to the heme iron of myoglobin. The distal E7 histidine hinders bonding of CO at the preferred (180 degree) angle to the plane of the heme ring. Figure 6-3. Angles for bonding of oxygen and carbon monoxide to the heme iron of myoglobin. The distal E7 histidine hinders bonding of CO at the preferred (180 degree) angle to the plane of the heme ring.
V. Srajer, T. Teng, T. Ursby, C. Pradervand, Z. Ren, S. Adachi, W. Schildkamp, D. Bourgeois, M. WuRf, and K. Moffat, Photolysis of the carbon monoxide complex of myoglobin nanosecond time-resolved crystallography. Science 274, 1726-1729 (1996). [Pg.284]

Elber, R. Karplus, M., Enhanced sampling in molecular-dynamics - use of the time-dependent Hartree approximation for a simulation of carbon-monoxide diffusion through myoglobin, J. Am. Chem. Soc. 1990,112, 9161-9175... [Pg.319]

X-ray crystallographic structures of myoglobin and hemoglobin were first completed in 19662 and 19753, respectively. Since then, many other X-ray crystallographic studies of deoxy- and oxy- as well as met-myoglobin and hemoglobin have been carried out.22,24 Additionally, researchers have studied the carbon monoxide bound moieties MbCO and HbCO as well as MbNO. Site-directed mutagenesis of residues near the active sites of Mb and Hb have yielded... [Pg.172]


See other pages where Carbon Monoxide myoglobin is mentioned: [Pg.807]    [Pg.405]    [Pg.200]    [Pg.92]    [Pg.73]    [Pg.471]    [Pg.807]    [Pg.405]    [Pg.200]    [Pg.92]    [Pg.73]    [Pg.471]    [Pg.1150]    [Pg.331]    [Pg.1150]    [Pg.482]    [Pg.40]    [Pg.41]    [Pg.86]    [Pg.282]    [Pg.66]    [Pg.579]    [Pg.803]    [Pg.98]    [Pg.238]    [Pg.125]    [Pg.182]    [Pg.185]    [Pg.74]    [Pg.220]    [Pg.49]    [Pg.344]    [Pg.146]    [Pg.349]    [Pg.356]    [Pg.365]    [Pg.377]   
See also in sourсe #XX -- [ Pg.349 , Pg.356 , Pg.357 , Pg.358 ]




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Carbon monoxide binding to hemoglobin and myoglobin

Carbon monoxide interaction with myoglobin

Carbon monoxide myoglobin MbCO)

Carbon monoxide myoglobin water

Myoglobin

Myoglobin carbon monoxide binding

Myoglobin-carbon monoxide reaction

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